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Bacterial lectins: multivalent proteins interacting with glycosylated surfaces and nanomaterials: Dr Anne Imberty

November 12, 2013 @ 10:00 am - 11:00 am

A large number of pathogenic microorganisms display receptors for specific recognition and adhesion to the glycoconjugates present on human tissues. In addition to membrane-bound adhesins, soluble lectins are involved in infections caused by the bacteria Pseudomonas aeruginosa and Burkholderia cepacia and by the fungus Aspergillus fumigatus that are responsible for hospital-acquired diseases. Accumulated knoweldge about the structures of the lectins and the interactions with host glycoconjugates has lead to the design of powerful glyco-derived inhibitors that can serve as antimicrobial therapeutic agents, as a complement to or an alternative to antibiotic therapy.

These soluble lectins present several binding sites with different architectures that make them perfect tools for studying the effect of multivalency on binding to surfaces or particles. Interactions with glycosylated chips, liposomes, fullerenes and gold nanoparticles have provided information about the effect of multivalency on avidity. Such nanomaterials can be used in diagnostic applications. The detection of lectin binding has been performed using devices based on glyco-functionalized carbon nanotubes or graphene incorporated in a field effect transistor.


November 12, 2013
10:00 am - 11:00 am


Level 5 Seminar Room, Burlington Danes Building
Hammersmith Campus, London, W12 0NN


Imperial Faculty of Medicine

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